BMP6_HUMAN
ID BMP6_HUMAN Reviewed; 513 AA.
AC P22004; Q5TCP3;
DT 01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1991, sequence version 1.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Bone morphogenetic protein 6;
DE Short=BMP-6;
DE AltName: Full=VG-1-related protein;
DE Short=VG-1-R;
DE Short=VGR-1;
DE Flags: Precursor;
GN Name=BMP6; Synonyms=VGR;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Bone;
RX PubMed=2263636; DOI=10.1073/pnas.87.24.9843;
RA Celeste A.J., Iannazzi J.A., Taylor R.C., Hewick R.M., Rosen V., Wang E.A.,
RA Wozney J.M.;
RT "Identification of transforming growth factor beta family members present
RT in bone-inductive protein purified from bovine bone.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9843-9847(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [3]
RP FUNCTION.
RX PubMed=33021694; DOI=10.1007/s10456-020-09748-4;
RA Pulkkinen H.H., Kiema M., Lappalainen J.P., Toropainen A., Beter M.,
RA Tirronen A., Holappa L., Niskanen H., Kaikkonen M.U., Ylae-Herttuala S.,
RA Laakkonen J.P.;
RT "BMP6/TAZ-Hippo signaling modulates angiogenesis and endothelial cell
RT response to VEGF.";
RL Angiogenesis 24:129-144(2021).
RN [4]
RP VARIANTS [LARGE SCALE ANALYSIS] ASP-343 AND LEU-476.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 382-513.
RX PubMed=17924656; DOI=10.1021/bi700907k;
RA Allendorph G.P., Isaacs M.J., Kawakami Y., Izpisua Belmonte J.C., Choe S.;
RT "BMP-3 and BMP-6 structures illuminate the nature of binding specificity
RT with receptors.";
RL Biochemistry 46:12238-12247(2007).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 397-513, DISULFIDE BONDS,
RP GLYCOSYLATION AT ASN-454, INTERACTION WITH ACVR1 AND ACVR2B, AND FUNCTION.
RX PubMed=18070108; DOI=10.1111/j.1742-4658.2007.06187.x;
RA Saremba S., Nickel J., Seher A., Kotzsch A., Sebald W., Mueller T.D.;
RT "Type I receptor binding of bone morphogenetic protein 6 is dependent on N-
RT glycosylation of the ligand.";
RL FEBS J. 275:172-183(2008).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 410-513, DISULFIDE BONDS, AND
RP FUNCTION.
RX PubMed=31019025; DOI=10.1126/scitranslmed.aar4953;
RA Seeherman H.J., Berasi S.P., Brown C.T., Martinez R.X., Juo Z.S.,
RA Jelinsky S., Cain M.J., Grode J., Tumelty K.E., Bohner M., Grinberg O.,
RA Orr N., Shoseyov O., Eyckmans J., Chen C., Morales P.R., Wilson C.G.,
RA Vanderploeg E.J., Wozney J.M.;
RT "A BMP/activin A chimera is superior to native BMPs and induces bone repair
RT in nonhuman primates when delivered in a composite matrix.";
RL Sci. Transl. Med. 11:0-0(2019).
CC -!- FUNCTION: Growth factor of the TGF-beta superfamily that plays
CC essential roles in many developmental processes including cartilage and
CC bone formation (PubMed:31019025). Also plays an important role in the
CC regulation of iron metabolism by acting as a ligand for hemojuvelin/HJV
CC (By similarity). Initiates the canonical BMP signaling cascade by
CC associating with type I receptor ACVR1 and type II receptor ACVR2B
CC (PubMed:18070108). In turn, ACVR1 propagates signal by phosphorylating
CC SMAD1/5/8 that travel to the nucleus and act as activators and
CC repressors of transcription of target. Can also signal through non-
CC canonical pathway such as TAZ-Hippo signaling cascade to modulate VEGF
CC signaling by regulating VEGFR2 expression (PubMed:33021694).
CC {ECO:0000250|UniProtKB:P20722, ECO:0000269|PubMed:18070108,
CC ECO:0000269|PubMed:31019025, ECO:0000269|PubMed:33021694}.
CC -!- SUBUNIT: Interacts with SOSTDC1 (By similarity). Interacts (when
CC glycosylated) with type I receptor ACVR1 (PubMed:18070108). Interacts
CC with type II receptor ACVR2B (PubMed:18070108). Interacts with
CC Hemojuvelin/HJV (By similarity). {ECO:0000250|UniProtKB:P20722,
CC ECO:0000269|PubMed:18070108}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- PTM: Glycosylated at Asn-454. Glycosylation is crucial for recognition
CC by the activin receptor type I/ACVR1. {ECO:0000269|PubMed:18070108}.
CC -!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Wikipedia; Note=Bone morphogenetic protein 6 entry;
CC URL="https://en.wikipedia.org/wiki/Bone_morphogenetic_protein_6";
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DR EMBL; M60315; AAA36737.1; -; mRNA.
DR EMBL; AL135778; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS4503.1; -.
DR PIR; B39263; BMHU6.
DR RefSeq; NP_001709.1; NM_001718.5.
DR PDB; 2QCW; X-ray; 2.49 A; A/B=382-513.
DR PDB; 2R52; X-ray; 2.50 A; A/B=375-513.
DR PDB; 2R53; X-ray; 2.10 A; A/B=411-513.
DR PDB; 6OMO; X-ray; 2.80 A; I/J=410-513.
DR PDBsum; 2QCW; -.
DR PDBsum; 2R52; -.
DR PDBsum; 2R53; -.
DR PDBsum; 6OMO; -.
DR AlphaFoldDB; P22004; -.
DR SMR; P22004; -.
DR BioGRID; 107122; 15.
DR DIP; DIP-5797N; -.
DR IntAct; P22004; 1.
DR STRING; 9606.ENSP00000283147; -.
DR BindingDB; P22004; -.
DR ChEMBL; CHEMBL3286078; -.
DR GlyGen; P22004; 5 sites.
DR iPTMnet; P22004; -.
DR PhosphoSitePlus; P22004; -.
DR BioMuta; BMP6; -.
DR DMDM; 115076; -.
DR MassIVE; P22004; -.
DR MaxQB; P22004; -.
DR PaxDb; P22004; -.
DR PeptideAtlas; P22004; -.
DR PRIDE; P22004; -.
DR ProteomicsDB; 53952; -.
DR Antibodypedia; 3456; 448 antibodies from 37 providers.
DR DNASU; 654; -.
DR Ensembl; ENST00000283147.7; ENSP00000283147.6; ENSG00000153162.9.
DR GeneID; 654; -.
DR KEGG; hsa:654; -.
DR MANE-Select; ENST00000283147.7; ENSP00000283147.6; NM_001718.6; NP_001709.1.
DR UCSC; uc003mxu.5; human.
DR CTD; 654; -.
DR DisGeNET; 654; -.
DR GeneCards; BMP6; -.
DR HGNC; HGNC:1073; BMP6.
DR HPA; ENSG00000153162; Tissue enhanced (placenta).
DR MalaCards; BMP6; -.
DR MIM; 112266; gene.
DR neXtProt; NX_P22004; -.
DR OpenTargets; ENSG00000153162; -.
DR PharmGKB; PA25383; -.
DR VEuPathDB; HostDB:ENSG00000153162; -.
DR eggNOG; KOG3900; Eukaryota.
DR GeneTree; ENSGT00940000158768; -.
DR HOGENOM; CLU_020515_4_1_1; -.
DR InParanoid; P22004; -.
DR OMA; ERQQPWP; -.
DR OrthoDB; 1063560at2759; -.
DR PhylomeDB; P22004; -.
DR TreeFam; TF316134; -.
DR PathwayCommons; P22004; -.
DR SignaLink; P22004; -.
DR BioGRID-ORCS; 654; 11 hits in 1070 CRISPR screens.
DR ChiTaRS; BMP6; human.
DR EvolutionaryTrace; P22004; -.
DR GeneWiki; Bone_morphogenetic_protein_6; -.
DR GenomeRNAi; 654; -.
DR Pharos; P22004; Tbio.
DR PRO; PR:P22004; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; P22004; protein.
DR Bgee; ENSG00000153162; Expressed in secondary oocyte and 122 other tissues.
DR Genevisible; P22004; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0031982; C:vesicle; IEA:Ensembl.
DR GO; GO:0070700; F:BMP receptor binding; IDA:MGI.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IDA:MGI.
DR GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
DR GO; GO:0051216; P:cartilage development; IEA:UniProtKB-KW.
DR GO; GO:0006879; P:cellular iron ion homeostasis; ISS:BHF-UCL.
DR GO; GO:0071773; P:cellular response to BMP stimulus; IMP:BHF-UCL.
DR GO; GO:0071281; P:cellular response to iron ion; ISS:BHF-UCL.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
DR GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
DR GO; GO:0001654; P:eye development; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; IMP:BHF-UCL.
DR GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0030539; P:male genitalia development; IEA:Ensembl.
DR GO; GO:0060586; P:multicellular organismal iron ion homeostasis; ISS:BHF-UCL.
DR GO; GO:1903392; P:negative regulation of adherens junction organization; IDA:ARUK-UCL.
DR GO; GO:2000048; P:negative regulation of cell-cell adhesion mediated by cadherin; IDA:ARUK-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0030182; P:neuron differentiation; IEA:Ensembl.
DR GO; GO:0001649; P:osteoblast differentiation; IEA:Ensembl.
DR GO; GO:0032349; P:positive regulation of aldosterone biosynthetic process; IDA:UniProtKB.
DR GO; GO:2000860; P:positive regulation of aldosterone secretion; IEA:Ensembl.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:BHF-UCL.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:BHF-UCL.
DR GO; GO:0032332; P:positive regulation of chondrocyte differentiation; IEA:Ensembl.
DR GO; GO:0045603; P:positive regulation of endothelial cell differentiation; IEA:Ensembl.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IEA:Ensembl.
DR GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:BHF-UCL.
DR GO; GO:0010628; P:positive regulation of gene expression; IMP:ARUK-UCL.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:BHF-UCL.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:BHF-UCL.
DR GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; IDA:UniProtKB.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:ARUK-UCL.
DR GO; GO:0050714; P:positive regulation of protein secretion; NAS:BHF-UCL.
DR GO; GO:0060391; P:positive regulation of SMAD protein signal transduction; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0043117; P:positive regulation of vascular permeability; IDA:ARUK-UCL.
DR GO; GO:0014823; P:response to activity; IEA:Ensembl.
DR GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
DR GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
DR GO; GO:0032526; P:response to retinoic acid; IEA:Ensembl.
DR GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
DR GO; GO:0060395; P:SMAD protein signal transduction; IDA:UniProtKB.
DR GO; GO:0003323; P:type B pancreatic cell development; IDA:BHF-UCL.
DR Gene3D; 2.10.90.10; -; 1.
DR InterPro; IPR029034; Cystine-knot_cytokine.
DR InterPro; IPR001839; TGF-b_C.
DR InterPro; IPR001111; TGF-b_propeptide.
DR InterPro; IPR015615; TGF-beta-rel.
DR InterPro; IPR017948; TGFb_CS.
DR PANTHER; PTHR11848; PTHR11848; 1.
DR Pfam; PF00019; TGF_beta; 1.
DR Pfam; PF00688; TGFb_propeptide; 1.
DR SMART; SM00204; TGFB; 1.
DR SUPFAM; SSF57501; SSF57501; 1.
DR PROSITE; PS00250; TGF_BETA_1; 1.
DR PROSITE; PS51362; TGF_BETA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chondrogenesis; Cleavage on pair of basic residues; Cytokine;
KW Developmental protein; Differentiation; Disulfide bond; Glycoprotein;
KW Growth factor; Osteogenesis; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT PROPEP 21..374
FT /evidence="ECO:0000255"
FT /id="PRO_0000033870"
FT CHAIN 375..513
FT /note="Bone morphogenetic protein 6"
FT /id="PRO_0000033871"
FT REGION 38..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 89..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..200
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..174
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 382..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 269
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 386
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 404
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 454
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255, ECO:0000269|PubMed:18070108"
FT DISULFID 412..478
FT /evidence="ECO:0000269|PubMed:18070108,
FT ECO:0000269|PubMed:31019025"
FT DISULFID 441..510
FT /evidence="ECO:0000269|PubMed:18070108,
FT ECO:0000269|PubMed:31019025"
FT DISULFID 445..512
FT /evidence="ECO:0000269|PubMed:18070108,
FT ECO:0000269|PubMed:31019025"
FT DISULFID 477
FT /note="Interchain"
FT /evidence="ECO:0000269|PubMed:18070108,
FT ECO:0000269|PubMed:31019025"
FT VARIANT 257
FT /note="R -> C (in dbSNP:rs10458105)"
FT /id="VAR_047055"
FT VARIANT 343
FT /note="A -> D (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036200"
FT VARIANT 476
FT /note="P -> L (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs909733732)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036201"
FT STRAND 411..415
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 418..420
FT /evidence="ECO:0007829|PDB:2R53"
FT TURN 421..425
FT /evidence="ECO:0007829|PDB:2R53"
FT TURN 427..429
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 430..432
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 440..442
FT /evidence="ECO:0007829|PDB:2R53"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:2R53"
FT HELIX 457..468
FT /evidence="ECO:0007829|PDB:2R53"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 477..491
FT /evidence="ECO:0007829|PDB:2R53"
FT STRAND 497..513
FT /evidence="ECO:0007829|PDB:2R53"
SQ SEQUENCE 513 AA; 57226 MW; 3F19155B36049278 CRC64;
MPGLGRRAQW LCWWWGLLCS CCGPPPLRPP LPAAAAAAAG GQLLGDGGSP GRTEQPPPSP
QSSSGFLYRR LKTQEKREMQ KEILSVLGLP HRPRPLHGLQ QPQPPALRQQ EEQQQQQQLP
RGEPPPGRLK SAPLFMLDLY NALSADNDED GASEGERQQS WPHEAASSSQ RRQPPPGAAH
PLNRKSLLAP GSGSGGASPL TSAQDSAFLN DADMVMSFVN LVEYDKEFSP RQRHHKEFKF
NLSQIPEGEV VTAAEFRIYK DCVMGSFKNQ TFLISIYQVL QEHQHRDSDL FLLDTRVVWA
SEEGWLEFDI TATSNLWVVT PQHNMGLQLS VVTRDGVHVH PRAAGLVGRD GPYDKQPFMV
AFFKVSEVHV RTTRSASSRR RQQSRNRSTQ SQDVARVSSA SDYNSSELKT ACRKHELYVS
FQDLGWQDWI IAPKGYAANY CDGECSFPLN AHMNATNHAI VQTLVHLMNP EYVPKPCCAP
TKLNAISVLY FDDNSNVILK KYRNMVVRAC GCH
